Activity-based proteomics uncovers suppressed hydrolases and a neo-functionalised antibacterial enzyme at the plant-pathogen interface

© 2023 The Authors New Phytologist © 2023 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 241(2024), 1 vom: 04. Jan., Seite 394-408
1. Verfasser: Sueldo, Daniela J (VerfasserIn)
Weitere Verfasser: Godson, Alice, Kaschani, Farnusch, Krahn, Daniel, Kessenbrock, Till, Buscaill, Pierre, Schofield, Christopher J, Kaiser, Markus, van der Hoorn, Renier A L
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Nicotiana benthamiana PR3 Pseudomonas syringae activity-based proteomics apoplast chitinase glycosidase hydrolases Hydrolases mehr... EC 3.- Chitinases EC 3.2.1.14
Beschreibung
Zusammenfassung:© 2023 The Authors New Phytologist © 2023 New Phytologist Foundation.
The extracellular space of plant tissues contains hundreds of hydrolases that might harm colonising microbes. Successful pathogens may suppress these hydrolases to enable disease. Here, we report the dynamics of extracellular hydrolases in Nicotiana benthamiana upon infection with Pseudomonas syringae. Using activity-based proteomics with a cocktail of biotinylated probes, we simultaneously monitored 171 active hydrolases, including 109 serine hydrolases (SHs), 49 glycosidases (GHs) and 13 cysteine proteases (CPs). The activity of 82 of these hydrolases (mostly SHs) increases during infection, while the activity of 60 hydrolases (mostly GHs and CPs) is suppressed during infection. Active β-galactosidase-1 (BGAL1) is amongst the suppressed hydrolases, consistent with production of the BGAL1 inhibitor by P. syringae. One of the other suppressed hydrolases, the pathogenesis-related NbPR3, decreases bacterial growth when transiently overexpressed. This is dependent on its active site, revealing a role for NbPR3 activity in antibacterial immunity. Despite being annotated as a chitinase, NbPR3 does not possess chitinase activity and contains an E112Q active site substitution that is essential for antibacterial activity and is present only in Nicotiana species. This study introduces a powerful approach to reveal novel components of extracellular immunity, exemplified by the discovery of the suppression of neo-functionalised Nicotiana-specific antibacterial NbPR3
Beschreibung:Date Completed 11.12.2023
Date Revised 22.03.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.18857